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Copper-zinc superoxide dismutase from Ascaris suum (Nematoda) was purified in a new, more efficient, and faster manner. The process included differential centrifugation, fractionation with ammonium sulfate, and sodium dodecyl sulfate-polyacrylamide electrophoresis, yielding a 340-fold purification (specific activity of 47 units/mg). Optimal storage conditions, optimal pH range, thermostability, molecular weight and ultraviolet-visible absorption spectrum of the enzyme are described, and a new enzymatic model for pharmacological screening is suggested.
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